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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
1999-3-23
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pubmed:abstractText |
The nature of the proteinaceous film deposited on a biomaterial surface following implantation is a key determinant of the subsequent biological response. To achieve selectivity in the formation of this film, monoclonal antibodies have been coupled to a range of solid substrates using avidin-biotin technology. Antibody clones varied in their antigen-binding activity following insertion of biotin groups into lysine residues. Biotinylated antibodies coupled to solid substrates via an immobilized avidin bridge retained their biological activity. During immobilization of avidin a significant proportion of the protein molecules were passively adsorbed rather than covalently attached to the surface. This loosely bound material could be removed by stringent elution procedures which resulted in a surface density of 5.4 pmol avidin cm(-2). Although these conditions would be harsh enough to denature monoclonal antibodies, they did not destroy the biotin-binding activity of the residual surface-coupled avidin, enabling the subsequent immobilization of biotinylated antibodies. The two-step immobilization technique allowed the use of gentle protein modification procedures, reduced the risk of surface-induced denaturation and removed loosely bound material from the surface. The versatility of the technique encourages its application to a wide range of immobilization systems where retention of biological activity is a key requirement.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Avidin,
http://linkedlifedata.com/resource/pubmed/chemical/Biotin,
http://linkedlifedata.com/resource/pubmed/chemical/Coated Materials, Biocompatible,
http://linkedlifedata.com/resource/pubmed/chemical/Collodion,
http://linkedlifedata.com/resource/pubmed/chemical/Membranes, Artificial,
http://linkedlifedata.com/resource/pubmed/chemical/Polytetrafluoroethylene,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin
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pubmed:status |
MEDLINE
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pubmed:issn |
0920-5063
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1207-25
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pubmed:dateRevised |
2008-2-20
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pubmed:meshHeading |
pubmed-meshheading:9860181-Adsorption,
pubmed-meshheading:9860181-Animals,
pubmed-meshheading:9860181-Antibodies, Monoclonal,
pubmed-meshheading:9860181-Avidin,
pubmed-meshheading:9860181-Biotin,
pubmed-meshheading:9860181-Coated Materials, Biocompatible,
pubmed-meshheading:9860181-Collodion,
pubmed-meshheading:9860181-Female,
pubmed-meshheading:9860181-Humans,
pubmed-meshheading:9860181-Membranes, Artificial,
pubmed-meshheading:9860181-Mice,
pubmed-meshheading:9860181-Mice, Inbred BALB C,
pubmed-meshheading:9860181-Polytetrafluoroethylene,
pubmed-meshheading:9860181-Serum Albumin,
pubmed-meshheading:9860181-Surface Properties
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pubmed:year |
1998
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pubmed:articleTitle |
Albumin-binding surfaces: synthesis and characterization.
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pubmed:affiliation |
Cooperative Research Centre for Cardiac Technology, CSIRO Molecular Science, Sydney Laboratory, North Ryde, NSW, Australia.
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pubmed:publicationType |
Journal Article
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